Daniel S. Johnson
Hofstra University
20 Papers
98 Citations
Daniel S. Johnson is an academic researcher from Hofstra University. The author has contributed to research in topics: ESCRT & Nuclear pore. The author has an hindex of 10, co-authored 20 publications. Previous affiliations of Daniel S. Johnson include Howard Hughes Medical Institute & Sandia National Laboratories.
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Papers
Synergistic action of RNA polymerases in overcoming the nucleosomal barrier
Jing Jin,Jing Jin,Lu Bai,Lu Bai,Daniel S. Johnson,Daniel S. Johnson,Robert M. Fulbright,Maria L. Kireeva,Mikhail Kashlev,Michelle D. Wang,Michelle D. Wang +10 more
TL;DR: The data indicate that histone-DNA interactions dictate RNAP pausing behavior, and alleviation of nucleosome-induced backtracking by multiple polymerases may prove to be a mechanism for overcoming the nucleosomal barrier in vivo.
Temporal and spatial organization of ESCRT protein recruitment during HIV-1 budding
Marina Bleck,Michelle S. Itano,Daniel S. Johnson,V. Kaye Thomas,Alison J. North,Paul D. Bieniasz,Sanford M. Simon +6 more
TL;DR: Investigation of how the virus hijacks cellular proteins to enable the release of virions from an infected cell shows with high temporal and spatial resolution that components of the host endosomal sorting complex required for transport (ESCRT) machinery are recruited to the neck of the assembling virus to facilitate scission of the link between the virus and the cell.
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ATP-induced helicase slippage reveals highly coordinated subunits
Bo Sun,Bo Sun,Daniel S. Johnson,Daniel S. Johnson,Daniel S. Johnson,Gayatri Patel,Benjamin Y. Smith,Benjamin Y. Smith,Manjula Pandey,Smita S. Patel,Michelle D. Wang,Michelle D. Wang +11 more
TL;DR: Wang et al. as discussed by the authors used a single-molecule approach to monitor the behavior of hexameric helicase in the presence of ATP and deoxythymine triphosphate (dTTP).
Timing of ESCRT-III protein recruitment and membrane scission during HIV-1 assembly
TL;DR: Observations suggest that ESCRT-IIIs are recruited by a combination of membrane curvature and the late domains of the HIV-1 Gag protein, which is likely relevant for other ESC RT-dependent scission processes including cell division, endosome tubulation, multivesicular body and nuclear envelope formation, and secretion of exosomes and ectosomes.
Direct determination of particle-particle interactions in a 2D plasma dust crystal.
TL;DR: Particle interactions were directly determined from the lateral compression of two-dimensional plasma dust crystals confined in a parabolic potential well using measured particle separations combined with an equation of state for the crystal to derive values for the particle screening length and the charge.
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